共查询到20条相似文献,搜索用时 15 毫秒
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Differential localization of HDAC4 orchestrates muscle differentiation 总被引:11,自引:0,他引:11
Miska EA Langley E Wolf D Karlsson C Pines J Kouzarides T 《Nucleic acids research》2001,29(16):3439-3447
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Like the full-length histone deacetylase (HDAC) 4, its amino terminus (amino acids 1-208) without the carboxyl deacetylase domain is also known to effectively bind and repress myocyte enhancer factor 2 (MEF2). Within this repressive amino terminus, we further show that a stretch of 90 amino acids (119-208) displays MEF2 binding and repressive activity. The same region is also found to associate specifically with HDAC1 which is responsible for the repressive effect. The amino terminus of HDAC4 can associate with the DNA-bound MEF2 in vitro, suggesting that it does not repress MEF2 simply by disrupting the ability of MEF2 to bind DNA. In vivo, MEF2 induces nuclear translocation of both the full-length HDAC4 and HDAC4-(1-208), whereas the nuclear HDAC4 as well as HDAC4-(1-208) in turn specifically sequesters MEF2 to distinct nuclear bodies. In addition, we show that MyoD and HDAC4 functionally antagonize each other to regulate MEF2 activity. Combined with data from others, our data suggest that the full-length HDAC4 can repress MEF2 through multiple independent repressive domains. 相似文献
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Grégoire S Xiao L Nie J Zhang X Xu M Li J Wong J Seto E Yang XJ 《Molecular and cellular biology》2007,27(4):1280-1295
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HDAC4 deacetylase associates with and represses the MEF2 transcription factor. 总被引:28,自引:0,他引:28
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E A Miska C Karlsson E Langley S J Nielsen J Pines T Kouzarides 《The EMBO journal》1999,18(18):5099-5107
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Linseman DA Bartley CM Le SS Laessig TA Bouchard RJ Meintzer MK Li M Heidenreich KA 《The Journal of biological chemistry》2003,278(42):41472-41481
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Caspase cleavage of vimentin disrupts intermediate filaments and promotes apoptosis. 总被引:15,自引:0,他引:15
Y Byun F Chen R Chang M Trivedi K J Green V L Cryns 《Cell death and differentiation》2001,8(5):443-450
Caspases are key mediators of apoptosis. Using a novel expression cloning strategy we recently developed to identify cDNAs encoding caspase substrates, we isolated the intermediate filament protein vimentin as a caspase substrate. Vimentin is preferentially cleaved by multiple caspases at distinct sites in vitro, including Asp85 by caspases-3 and -7 and Asp259 by caspase-6, to yield multiple proteolytic fragments. Vimentin is rapidly proteolyzed by multiple caspases into similar sized fragments during apoptosis induced by many stimuli. Caspase cleavage of vimentin disrupts its cytoplasmic network of intermediate filaments and coincides temporally with nuclear fragmentation. Moreover, caspase proteolysis of vimentin at Asp85 generates a pro-apoptotic amino-terminal fragment whose ability to induce apoptosis is dependent on caspases. Taken together, our findings suggest that caspase proteolysis of vimentin promotes apoptosis by dismantling intermediate filaments and by amplifying the cell death signal via a pro-apoptotic cleavage product. 相似文献